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Enzyme Nomenclature
Information on EC 1.14.13.128 - 7-methylxanthine demethylase
Word Map on EC 1.14.13.128
- 1.14.13.128
- theophylline
-
alkaloid
- putida
-
bioreactors
- formaldehyde
- coffee
-
demethylation
-
bioprocess
- purine
- 3-methylxanthine
-
broad-specificity
-
rieske
-
oxygen-dependent
- paraxanthine
- aminopyrine
-
monooxygenase
- methylxanthines
- pharmacology
- medicine
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The expected taxonomic range for this enzyme is: Pseudomonas putida
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EC NUMBER 
COMMENTARY 
1.14.13.128
-
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RECOMMENDED NAME
GeneOntology No.
7-methylxanthine demethylase
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
7-methylxanthine + O2 + NAD(P)H + H+ = xanthine + NAD(P)+ + H2O + formaldehyde
-
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
7-methylxanthine:oxygen oxidoreductase (demethylating)
A non-heme iron oxygenase. The enzyme from the bacterium Pseudomonas putida prefers NADH over NADPH. The enzyme is specific for 7-methylxanthine [2]. Forms part of the caffeine degradation pathway.
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
-
catabolism of caffeine in microorganisms commences via two possible mechanisms: demethylation and oxidation. Through the demethylation route, the major metabolite formed in fungi is theophylline, whereas theobromine is the major metabolite in bacteria
metabolism
-
catabolism of caffeine in microorganisms commences via two possible mechanisms: demethylation and oxidation. Through the demethylation route, the major metabolite formed in fungi is theophylline, whereas theobromine is the major metabolite in bacteria. Catabolism of caffeine in microorganisms, overview
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
1,3,7-trimethylxanthine + O2 + NAD(P)H + H+
3,7-dimethylxanthine + formaldehyde + NAD(P)+
-
i.e. caffeine
i.e. theobromine
-
-
1,3,7-trimethylxanthine + O2 + NADPH + H+
1,3-dimethylxanthine + formaldehyde + NADP+ + H2O
-
i.e. caffeine
i.e. theophylline
-
-
1,3,7-trimethylxanthine + O2 + NADPH + H+
1,7-dimethylxanthine + formaldehyde + NADP+ + H2O
-
i.e. caffeine
i.e. paraxanthine
-
-
1,7-dimethylxanthine + O2 + NADPH + H+
7-methylxanthine + NADP+ + H2O + formaldehyde
-
i.e. paraxanthine, activity of the reductase component of the N-demethylase holoenzyme (Ccr) with NADPH is 22% of that with NADH. The enzyme also catalyzes the further demethylation of the product 7-methylxanthine to xanthine. Activity is absolutely dependent of oxygen as a cosubstrate
-
-
?
3,7-dimethylxanthine + O2 + NAD(P)H + H+
monomethylxanthine + formaldehyde + NADP+
-
theobromine demethylase
-
-
?
3-methylxanthine + O2 + NADH + H+
xanthine + NAD+ + H2O + formaldehyde
-
3-methylxanthine demethylation is 12% of the activity compared to demethylation of 7-methylxanthine. Activity is absolutely dependent of oxygen as a cosubstrate
-
-
?
7-methylxanthine + O2 + NAD(P)H + H+
xanthine + formaldehyde + NADP+
-
heteroxanthine demethylase, substrate-selective
-
-
?
7-methylxanthine + O2 + NADPH + H+
xanthine + NADP+ + H2O + formaldehyde
-
-
-
-
?
caffeine + 2 O2 + 2 NADH + 2 H+
7-methylxanthine + 2 NAD+ + 2 H2O + 2 formaldehyde
-
i.e. 1,3,7-trimethylxanthine. Caffeine demethylation is 7% of the activity compared to demethylation of 7-methylxanthine. Activity is absolutely dependent of oxygen as a cosubstrate
-
-
?
caffeine + 3 O2 + 3 NADH + 3 H+
xanthine + 3 NAD+ + 3 H2O + 3 formaldehyde
-
i.e. 1,3,7-trimethylxanthine. Caffeine demethylation is 7% of the activity compared to demethylation of 7-methylxanthine. Activity is absolutely dependent of oxygen as a cosubstrate
-
-
?
caffeine + O2 + NADH + H+
1,7-dimethylxanthine + NAD+ + H2O + formaldehyde
-
i.e. 1,3,7-trimethylxanthine. Caffeine demethylation is 7% of the activity compared to demethylation of 7-methylxanthine. Activity is absolutely dependent of oxygen as a cosubstrate
-
-
?
caffeine + O2 + NADH + H+
theobromine + NAD+ + H2O + formaldehyde
-
i.e. 1,3,7-trimethylxanthine. Caffeine demethylation is 7% of the activity compared to demethylation of 7-methylxanthine. Activity is absolutely dependent of oxygen as a cosubstrate
-
-
?
theobromine + 2 O2 + 2 NADH + 2 H+
xanthine + 2 NAD+ + 2 H2O + 2 formaldehyde
-
i.e. 3,7-dimethylxanthine. Theobromine demethylation is 13% of the activity compared to demethylation of 7-methylxanthine. Activity is absolutely dependent of oxygen as a cosubstrate
-
-
?
theobromine + O2 + NADH + H+
3-methylxanthine + NAD+ + H2O + formaldehyde
-
i.e. 3,7-dimethylxanthine. Theobromine demethylation is 13% of the activity compared to demethylation of 7-methylxanthine. Activity is absolutely dependent of oxygen as a cosubstrate
-
-
?
theobromine + O2 + NADH + H+
7-methylxanthine + NAD+ + H2O + formaldehyde
-
i.e. 3,7-dimethylxanthine. Theobromine demethylation is 13% of the activity compared to demethylation of 7-methylxanthine. Activity is absolutely dependent of oxygen as a cosubstrate
-
-
?
theophylline + 2 O2 + 2 NADH + 2 H+
xanthine + 2 NAD+ + 2 H2O + 2 formaldehyde
-
1,3-dimethylxanthine. Theophylline demethylation is 3% of the activity compared to demethylation of 7-methylxanthine. Activity is absolutely dependent of oxygen as a cosubstrate
-
-
?
theophylline + O2 + NADH + H+
1-methylxanthine + NAD+ + H2O + formaldehyde
-
1,3-dimethylxanthine. Theophylline demethylation is 3% of the activity compared to demethylation of 7-methylxanthine. Activity is absolutely dependent of oxygen as a cosubstrate
-
-
?
theophylline + O2 + NADH + H+
3-methylxanthine + NAD+ + H2O + formaldehyde
-
1,3-dimethylxanthine. Theophylline demethylation is 3% of the activity compared to demethylation of 7-methylxanthine. Activity is absolutely dependent of oxygen as a cosubstrate
-
-
?
1,7-dimethylxanthine + 2 O2 + 2 NADH + 2 H+
xanthine + 2 NAD+ + 2 H2O + 2 formaldehyde
-
i.e. paraxanthine, NADH is the preferred cofactor of reductase component of the N-demethylase holoenzyme (Ccr). The product 7-methylxanthine is further demethylated to xanthine. 1,7-Dimethylxanthine (paraxanthine) demethylation is 22% of the activity compared to demethylation of 7-methylxanthine. Activity is absolutely dependent of oxygen as a cosubstrate
-
-
?
1,7-dimethylxanthine + 2 O2 + 2 NADH + 2 H+
xanthine + 2 NAD+ + 2 H2O + 2 formaldehyde
-
i.e. paraxanthine, NADH is the preferred cofactor of reductase component of the N-demethylase holoenzyme (Ccr). The product 7-methylxanthine is further demethylated to xanthine. 1,7-Dimethylxanthine (paraxanthine) demethylation is 22% of the activity compared to demethylation of 7-methylxanthine. Activity is absolutely dependent of oxygen as a cosubstrate
-
-
?
1,7-dimethylxanthine + 2 O2 + 2 NADPH + 2 H+
xanthine + 2 NADP+ + 2 H2O + 2 formaldehyde
-
i.e. paraxanthine, activity of the reductase component of the N-demethylase holoenzyme (Ccr) with NADPH is 22% of that with NADH. The enzyme also catalyzes the further demethylation of the product 7-methylxanthine to xanthine. Activity is absolutely dependent of oxygen as a cosubstrate
-
-
?
1,7-dimethylxanthine + 2 O2 + 2 NADPH + 2 H+
xanthine + 2 NADP+ + 2 H2O + 2 formaldehyde
-
i.e. paraxanthine, activity of the reductase component of the N-demethylase holoenzyme (Ccr) with NADPH is 22% of that with NADH. The enzyme also catalyzes the further demethylation of the product 7-methylxanthine to xanthine. Activity is absolutely dependent of oxygen as a cosubstrate
-
-
?
1,7-dimethylxanthine + O2 + NADH + H+
7-methylxanthine + NAD+ + H2O + formaldehyde
-
i.e. paraxanthine, NADH is the preferred cofactor of reductase component of the N-demethylase holoenzyme (Ccr). The product 7-methylxanthine is further demethylated to xanthine. 1,7-Dimethylxanthine (paraxanthine) demethylation is 22% of the activity compared to demethylation of 7-methylxanthine. Activity is absolutely dependent of oxygen as a cosubstrate
-
-
?
1,7-dimethylxanthine + O2 + NADH + H+
7-methylxanthine + NAD+ + H2O + formaldehyde
-
i.e. paraxanthine, NADH is the preferred cofactor of reductase component of the N-demethylase holoenzyme (Ccr). The product 7-methylxanthine is further demethylated to xanthine. 1,7-Dimethylxanthine (paraxanthine) demethylation is 22% of the activity compared to demethylation of 7-methylxanthine. Activity is absolutely dependent of oxygen as a cosubstrate
-
-
?
7-methylxanthine + O2 + NAD(P)H + H+
xanthine + NAD(P)+ + H2O + formaldehyde
-
part of the caffeine degradation pathway in Pseudomonas putida
-
-
?
7-methylxanthine + O2 + NAD(P)H + H+
xanthine + NAD(P)+ + H2O + formaldehyde
-
part of the caffeine degradation pathway in Pseudomonas putida
-
-
?
7-methylxanthine + O2 + NADH + H+
xanthine + NAD+ + H2O + formaldehyde
-
-
-
-
?
7-methylxanthine + O2 + NADH + H+
xanthine + NAD+ + H2O + formaldehyde
specific substrate
-
-
?
7-methylxanthine + O2 + NADH + H+
xanthine + NAD+ + H2O + formaldehyde
-
the enzyme most actively demethylates 7-methylxanthine. Activity is absolutely dependent of oxygen as a cosubstrate
-
-
?
7-methylxanthine + O2 + NADH + H+
xanthine + NAD+ + H2O + formaldehyde
-
the N7-demethylation reaction absolutely requires a unique, tightly bound protein complex composed of NdmC, NdmD, and NdmE. NdmE functions as a noncatalytic subunit that serves a structural role in the complexation of the oxygenase (NdmC) and Rieske domains (NdmD)
-
-
?
7-methylxanthine + O2 + NADH + H+
xanthine + NAD+ + H2O + formaldehyde
specific substrate
-
-
?
7-methylxanthine + O2 + NADH + H+
xanthine + NAD+ + H2O + formaldehyde
-
the N7-demethylation reaction absolutely requires a unique, tightly bound protein complex composed of NdmC, NdmD, and NdmE. NdmE functions as a noncatalytic subunit that serves a structural role in the complexation of the oxygenase (NdmC) and Rieske domains (NdmD)
-
-
?
additional information
?
-
-
Ndm exhibits broad-based activity towards caffeine, theophylline, theobromine, 7-methylxanthine and 3-methylxanthine, all of which are growth substrates for Pseudomonas putida CBB5. Production of xanthine from all of these methylxanthines is confirmed. Ndm is most active on 7-methylxanthine, followed by 1,7-dimethylxanthine (paraxanthine), theobromine, 3-methylxanthine, caffeine and theophylline. Ndm does not catalyse O-demethylation of vanillate or vanillin, even after prolonged incubation
-
-
-
additional information
?
-
-
the metabolite is 1,3-dimethylxanthine, i.e. theophylline, is produced by the demethylation in the 7th position of the purine ring, mainly in fungi, overview
-
-
-
additional information
?
-
-
no activity of the heteroxanthine demethylase, when either caffeine or dimethylxanthines are used as substrates
-
-
-
additional information
?
-
caffeine, paraxanthine, and theobromine are not demethylated by the enzyme
-
-
-
additional information
?
-
-
no activity toward caffeine or theobromine
-
-
-
additional information
?
-
-
Ndm exhibits broad-based activity towards caffeine, theophylline, theobromine, 7-methylxanthine and 3-methylxanthine, all of which are growth substrates for Pseudomonas putida CBB5. Production of xanthine from all of these methylxanthines is confirmed. Ndm is most active on 7-methylxanthine, followed by 1,7-dimethylxanthine (paraxanthine), theobromine, 3-methylxanthine, caffeine and theophylline. Ndm does not catalyse O-demethylation of vanillate or vanillin, even after prolonged incubation
-
-
-
additional information
?
-
caffeine, paraxanthine, and theobromine are not demethylated by the enzyme
-
-
-
additional information
?
-
-
no activity toward caffeine or theobromine
-
-
-
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
1,3,7-trimethylxanthine + O2 + NAD(P)H + H+
3,7-dimethylxanthine + formaldehyde + NAD(P)+
-
i.e. caffeine
i.e. theobromine
-
-
1,3,7-trimethylxanthine + O2 + NADPH + H+
1,3-dimethylxanthine + formaldehyde + NADP+ + H2O
-
i.e. caffeine
i.e. theophylline
-
-
1,3,7-trimethylxanthine + O2 + NADPH + H+
1,7-dimethylxanthine + formaldehyde + NADP+ + H2O
-
i.e. caffeine
i.e. paraxanthine
-
-
7-methylxanthine + O2 + NAD(P)H + H+
xanthine + NAD(P)+ + H2O + formaldehyde
-
part of the caffeine degradation pathway in Pseudomonas putida
-
-
?
7-methylxanthine + O2 + NAD(P)H + H+
xanthine + NAD(P)+ + H2O + formaldehyde
-
part of the caffeine degradation pathway in Pseudomonas putida
-
-
?
7-methylxanthine + O2 + NADH + H+
xanthine + NAD+ + H2O + formaldehyde
M1EY73
specific substrate
-
-
?
7-methylxanthine + O2 + NADH + H+
xanthine + NAD+ + H2O + formaldehyde
-
the N7-demethylation reaction absolutely requires a unique, tightly bound protein complex composed of NdmC, NdmD, and NdmE. NdmE functions as a noncatalytic subunit that serves a structural role in the complexation of the oxygenase (NdmC) and Rieske domains (NdmD)
-
-
?
7-methylxanthine + O2 + NADH + H+
xanthine + NAD+ + H2O + formaldehyde
M1EY73
specific substrate
-
-
?
7-methylxanthine + O2 + NADH + H+
xanthine + NAD+ + H2O + formaldehyde
-
the N7-demethylation reaction absolutely requires a unique, tightly bound protein complex composed of NdmC, NdmD, and NdmE. NdmE functions as a noncatalytic subunit that serves a structural role in the complexation of the oxygenase (NdmC) and Rieske domains (NdmD)
-
-
?
additional information
?
-
-
the metabolite is 1,3-dimethylxanthine, i.e. theophylline, is produced by the demethylation in the 7th position of the purine ring, mainly in fungi, overview
-
-
-
additional information
?
-
M1EY73
caffeine, paraxanthine, and theobromine are not demethylated by the enzyme
-
-
-
additional information
?
-
-
no activity toward caffeine or theobromine
-
-
-
additional information
?
-
M1EY73
caffeine, paraxanthine, and theobromine are not demethylated by the enzyme
-
-
-
additional information
?
-
-
no activity toward caffeine or theobromine
-
-
-
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NADPH
-
activity of Ccr (reductase component of the N-demethylase holoenzyme) with NADPH is 22% of that with NADH
NADH
-
preferred cofactor of Ccr (reductase component of the N-demethylase holoenzyme)
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe2+
-
preincubation of Ndm for 15 min with 1 mM Fe2+, followed by desalting, increases the iron content to 20.1 mol per mol hexameric N-demethylase component (Ndm) of the N-demethylase holoenzyme. After this treatment, Ndm specific activity increases about 6fold (when 50 mM Fe2+ is present in the enzyme reaction mixture). N-Demethylase component (Ndm) of the N-demethylase holoenzyme is deduced to be a Rieske [2Fe-2S]-domain containing non-haem iron oxygenase
Iron
Iron
-
a Rieske nonheme iron monooxygenase. The enzyme contains 2 mol of iron per mol of monomer
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Zn2+
-
theobromine demethylase enzyme is inhibited by Zn2+, which generates the accumulation of theobromine
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0504
1,7-dimethylxanthine
-
pH 7.5, 30°C, kinetic parameters for two-subunit N-demethylase component (Ndm), in the presence of saturating amounts of Ccr (reductase component with cytochrome c reductase activity) and 50 mM Fe2+
1.1
3,7-Dimethylxanthine
-
theobromine demethylase, pH and temperature not specified in the publication
0.0153
7-methylxanthine
-
in 50 mM potassium phosphate buffer (pH 7.5) at 30°C
0.0638
7-methylxanthine
-
pH 7.5, 30°C, kinetic parameters for two-subunit N-demethylase component (Ndm), in the presence of saturating amounts of Ccr (reductase component with cytochrome c reductase activity) and 50 mM Fe2+
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.27
1,7-dimethylxanthine
Pseudomonas putida
-
pH 7.5, 30°C, kinetic parameters for two-subunit N-demethylase component (Ndm), in the presence of saturating amounts of Ccr (reductase component with cytochrome c reductase activity) and 50 mM Fe2+
0.16
7-methylxanthine
Pseudomonas putida
-
in 50 mM potassium phosphate buffer (pH 7.5) at 30°C
1.58
7-methylxanthine
Pseudomonas putida
-
pH 7.5, 30°C, kinetic parameters for two-subunit N-demethylase component (Ndm), in the presence of saturating amounts of Ccr (reductase component with cytochrome c reductase activity) and 50 mM Fe2+
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
5.4
1,7-dimethylxanthine
Pseudomonas putida
-
pH 7.5, 30°C, kinetic parameters for two-subunit N-demethylase component (Ndm), in the presence of saturating amounts of Ccr (reductase component with cytochrome c reductase activity) and 50 mM Fe2+
6872
10.17
7-methylxanthine
Pseudomonas putida
-
in 50 mM potassium phosphate buffer (pH 7.5) at 30°C
2307
24.8
7-methylxanthine
Pseudomonas putida
-
pH 7.5, 30°C, kinetic parameters for two-subunit N-demethylase component (Ndm), in the presence of saturating amounts of Ccr (reductase component with cytochrome c reductase activity) and 50 mM Fe2+
2307
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.3
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30 - 35
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
41000
-
x * 41000, theobromine demethylase, SDS-PAGE, x * 36600-43500, caffeine demethylase complex, SDS-PAGE
240000
-
gel filtration, two-subunit N-demethylase component (Ndm) of the N-demethylase holoenzyme
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
the soluble N-demethylase holoenzyme is composed of two components, a reductase component with cytochrome c reductase activity (Ccr) and a two-subunit N-demethylase component (Ndm), the native Ndm enzyme is probably composed of the two subunits (40000 Da (NdmA) and 35000 Da (NdmB)) in a hexameric configuration
?
-
x * 41000, theobromine demethylase, SDS-PAGE, x * 36600-43500, caffeine demethylase complex, SDS-PAGE
?
-
the soluble N-demethylase holoenzyme is composed of two components, a reductase component with cytochrome c reductase activity (Ccr) and a two-subunit N-demethylase component (Ndm), the native Ndm enzyme is probably composed of the two subunits (40000 Da (NdmA) and 35000 Da (NdmB)) in a hexameric configuration; x * 67000, SDS-PAGE
-
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
stabilization can be achieved by addition of either glycerol (20%), bovine serum albumin (10 mg/ml), dithiothreitol (1 mM) or the substrate 7-methylxanthine (1 mM). Storage under nitrogen atmosphere has a stabilizing influence. The addition of caffeine (1 mM), dimethylxanthines (1 mM) and protease inhibitors (pepstatin A, PMSF, 0.1 mM) is without influence on stability
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80°C, two-subunit N-demethylase component (Ndm) of the N-demethylase holoenzyme is stable for over 1 month
-
4°C, 5 days, two-subunit N-demethylase component (Ndm) of the N-demethylase holoenzyme is stabel for at lewast 5 days
-
similar to caffeine demethylase, heteroxanthinedemethylase is also unstable and loss of activity occurs upon storage
-
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
purification of two-subunit N-demethylase component (Ndm) of the N-demethylase holoenzyme
-
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
-
methylxanthine intermediates of caffeine catabolism obtained by the action of N-demethylases have many applications. In medicine, theobromine and theophylline are used as diuretics, vasodilators, and myocardial stimulants. Monomethylxanthines can be converted to effective caffeine derivatives by chemical derivatization and hence can serve as interesting alternatives to caffeine. Xanthine also finds pharmaceutical application in drugs for treatment of asthma. The biotechnological potential of N-demethylases therefore lies not only in general decaffeination purposes but also in specific product recovery from caffeine
pharmacology
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methylxanthine intermediates of caffeine catabolism obtained by the action of N-demethylases have many applications. In medicine, theobromine and theophylline are used as diuretics, vasodilators, and myocardial stimulants. Monomethylxanthines can be converted to effective caffeine derivatives by chemical derivatization and hence can serve as interesting alternatives to caffeine. Xanthine also finds pharmaceutical application in drugs for treatment of asthma. The biotechnological potential of N-demethylases therefore lies not only in general decaffeination purposes but also in specific product recovery from caffeine
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